eF-site ID 1o3t-AB
PDB Code 1o3t
Chain A, B

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Title PROTEIN-DNA RECOGNITION AND DNA DEFORMATION REVEALED IN CRYSTAL STRUCTURES OF CAP-DNA COMPLEXES
Classification GENE REGULATION/DNA
Compound 5'-D(*GP*CP*GP*AP*AP*AP*AP*AP*TP*GP*CP*GP*AP*T)-3'
Source null (1O3T)
Sequence A:  PTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVA
VLIKDEEGKEMILSYLNQGDFIGELGLFEEGQERSAWVRA
KTACEVAEISYKKFRQLIQVNPDILMRLSAQMARRLQVTS
EKVGNLAFLDVTGRIAQTLLNLAKQPDAMTHPDGMQIKIT
RQEIGQIVGCSRETVGRILKMLEDQNLISAHGKTIVVYG
B:  PTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVA
VLIKDEEGKEMILSYLNQGDFIGELGLFEEGQERSAWVRA
KTACEVAEISYKKFRQLIQVNPDILMRLSAQMARRLQVTS
EKVGNLAFLDVTGRIAQTLLNLAKQPDAMTHPDGMQIKIT
RQEIGQIVGCSRETVGRILKMLEDQNLISAHGKTIVV
Description


Functional site
1) chain A
residue 124
type
sequence L
description BINDING SITE FOR RESIDUE CMP B 761
source : AC1
2) chain A
residue 128
type
sequence S
description BINDING SITE FOR RESIDUE CMP B 761
source : AC1
3) chain B
residue 30
type
sequence I
description BINDING SITE FOR RESIDUE CMP B 761
source : AC1
4) chain B
residue 49
type
sequence V
description BINDING SITE FOR RESIDUE CMP B 761
source : AC1
5) chain B
residue 62
type
sequence S
description BINDING SITE FOR RESIDUE CMP B 761
source : AC1
6) chain B
residue 71
type
sequence G
description BINDING SITE FOR RESIDUE CMP B 761
source : AC1
7) chain B
residue 72
type
sequence E
description BINDING SITE FOR RESIDUE CMP B 761
source : AC1
8) chain B
residue 73
type
sequence L
description BINDING SITE FOR RESIDUE CMP B 761
source : AC1
9) chain B
residue 82
type
sequence R
description BINDING SITE FOR RESIDUE CMP B 761
source : AC1
10) chain B
residue 83
type
sequence S
description BINDING SITE FOR RESIDUE CMP B 761
source : AC1
11) chain B
residue 84
type
sequence A
description BINDING SITE FOR RESIDUE CMP B 761
source : AC1
12) chain B
residue 123
type
sequence R
description BINDING SITE FOR RESIDUE CMP B 761
source : AC1
13) chain B
residue 127
type
sequence T
description BINDING SITE FOR RESIDUE CMP B 761
source : AC1
14) chain A
residue 49
type
sequence V
description BINDING SITE FOR RESIDUE CMP A 762
source : AC2
15) chain A
residue 61
type
sequence L
description BINDING SITE FOR RESIDUE CMP A 762
source : AC2
16) chain A
residue 70
type
sequence I
description BINDING SITE FOR RESIDUE CMP A 762
source : AC2
17) chain A
residue 71
type
sequence G
description BINDING SITE FOR RESIDUE CMP A 762
source : AC2
18) chain A
residue 72
type
sequence E
description BINDING SITE FOR RESIDUE CMP A 762
source : AC2
19) chain A
residue 73
type
sequence L
description BINDING SITE FOR RESIDUE CMP A 762
source : AC2
20) chain A
residue 82
type
sequence R
description BINDING SITE FOR RESIDUE CMP A 762
source : AC2
21) chain A
residue 83
type
sequence S
description BINDING SITE FOR RESIDUE CMP A 762
source : AC2
22) chain A
residue 84
type
sequence A
description BINDING SITE FOR RESIDUE CMP A 762
source : AC2
23) chain A
residue 127
type
sequence T
description BINDING SITE FOR RESIDUE CMP A 762
source : AC2
24) chain B
residue 124
type
sequence L
description BINDING SITE FOR RESIDUE CMP A 762
source : AC2
25) chain B
residue 128
type
sequence S
description BINDING SITE FOR RESIDUE CMP A 762
source : AC2
26) chain A
residue 179-185
type DNA_BIND
sequence SRETVGR
description H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00387
source Swiss-Prot : SWS_FT_FI1
27) chain B
residue 179-185
type DNA_BIND
sequence SRETVGR
description H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00387
source Swiss-Prot : SWS_FT_FI1
28) chain A
residue 56
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802
source Swiss-Prot : SWS_FT_FI2
29) chain A
residue 71
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802
source Swiss-Prot : SWS_FT_FI2
30) chain A
residue 82
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802
source Swiss-Prot : SWS_FT_FI2
31) chain A
residue 127
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802
source Swiss-Prot : SWS_FT_FI2
32) chain B
residue 127
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802
source Swiss-Prot : SWS_FT_FI2
33) chain B
residue 135
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802
source Swiss-Prot : SWS_FT_FI2
34) chain B
residue 170
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802
source Swiss-Prot : SWS_FT_FI2
35) chain A
residue 135
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802
source Swiss-Prot : SWS_FT_FI2
36) chain A
residue 170
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802
source Swiss-Prot : SWS_FT_FI2
37) chain B
residue 56
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802
source Swiss-Prot : SWS_FT_FI2
38) chain B
residue 71
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802
source Swiss-Prot : SWS_FT_FI2
39) chain B
residue 82
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802
source Swiss-Prot : SWS_FT_FI2
40) chain A
residue 100
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:18723842
source Swiss-Prot : SWS_FT_FI5
41) chain B
residue 100
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:18723842
source Swiss-Prot : SWS_FT_FI5
42) chain A
residue 96
type SITE
sequence E
description Activating region 2 (AR2); probably contacts the N-terminus of RpoA => ECO:0000269|PubMed:8978616
source Swiss-Prot : SWS_FT_FI3
43) chain B
residue 96
type SITE
sequence E
description Activating region 2 (AR2); probably contacts the N-terminus of RpoA => ECO:0000269|PubMed:8978616
source Swiss-Prot : SWS_FT_FI3
44) chain A
residue 167-190
type prosite
sequence ITRQEIGQIVGCSRETVGRILKML
description HTH_CRP_1 Crp-type HTH domain signature. ITRqeIGqIVGcSreTv.GRiLkmL
source prosite : PS00042
45) chain A
residue 29-45
type prosite
sequence LIHQGEKAETLYYIVKG
description CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. LIhQGEkAEtLYYIvkG
source prosite : PS00888
46) chain A
residue 70-88
type prosite
sequence IGELGLFEEGQERSAWVRA
description CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. IGElGLfeegqe.....RSAwVrA
source prosite : PS00889
47) chain A
residue 101
type SITE
sequence K
description Activating region 2 (AR2); probably contacts the N-terminus of RpoA => ECO:0000269|PubMed:15520470, ECO:0000269|PubMed:8978616
source Swiss-Prot : SWS_FT_FI4
48) chain B
residue 101
type SITE
sequence K
description Activating region 2 (AR2); probably contacts the N-terminus of RpoA => ECO:0000269|PubMed:15520470, ECO:0000269|PubMed:8978616
source Swiss-Prot : SWS_FT_FI4

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